Structural Transitions of Papain-like Cysteine Proteases: Implications for Sensor Development.

ABSTRACT: The significant role of papain-like cysteine proteases, including papain, cathepsin L and SARS-CoV-2 PLpro, in biomedicine and biotechnology makes them interesting model systems for sensor development. These enzymes have a free thiol group that is suitable for many sensor designs including strong binding to gold nanoparticles or low-molecular-weight inhibitors. Focusing on the importance of the preservation of native protein structure for inhibitor-binding and molecular-imprinting, which has been applied in some efficient examples of sensor development, the aim of this work was to examine the effects of the free-thiol-group's reversible blocking on papain denaturation that is the basis of its activity loss and aggregation. To utilize biophysical methods common in protein structural transit

SUBMITTER: Markovic S 

PROVIDER: S-EPMC10807080 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature